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Information on EC 1.3.3.15 - coproporphyrinogen III oxidase (coproporphyrin-forming)
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1.3.3.15 coproporphyrinogen III oxidase (coproporphyrin-forming)IUBMB Comments
Contains FAD. The enzyme, present in Gram-positive bacteria, participates in heme biosynthesis. It can also catalyse the reaction of EC 1.3.3.4, protoporphyrinogen oxidase, at a lower level.
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The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
CgoX, coproporphyrinogen III oxidase, coproporphyrinogen oxidase, hemY, PPO, proto'gen oxidase, protoporphyrinogen IX oxidase, protoporphyrinogen oxidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CgoX
coproporphyrinogen III oxidase
hemY
PPO
protoporphyrinogen IX oxidase
hemY
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
coproporphyrinogen III + 3 O2 = coproporphyrin III + 3 H2O2
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
coproporphyrinogen-III:oxygen oxidoreductase (coproporphyrin-forming)
Contains FAD. The enzyme, present in Gram-positive bacteria, participates in heme biosynthesis. It can also catalyse the reaction of EC 1.3.3.4, protoporphyrinogen oxidase, at a lower level.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
?
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
-
?
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
?
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
-
?
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
-
?
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
-
-
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
12fold higher catalytic efficiency with coproporphyrinogen III compared to protoporphyrinogen as substrate
-
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
-
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
12fold higher catalytic efficiency with coproporphyrinogen III compared to protoporphyrinogen as substrate
-
-
?
protoporphyrinogen IX + 3 O2
protoporphyrin IX + 3 H2O2
-
-
-
?
protoporphyrinogen IX + 3 O2
protoporphyrin IX + 3 H2O2
-
-
-
?
protoporphyrinogen IX + 3 O2
protoporphyrin IX + 3 H2O2
-
-
-
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
-
-
-
-
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
20fold lower activity with protoporphyrinogen IX compared to coproporphyrinogen III
-
-
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
20fold lower activity with protoporphyrinogen IX compared to coproporphyrinogen III
-
-
?
additional information
?
-
-
the enzyme does not oxidize uroporphyrinogen III
-
-
?
additional information
?
-
-
the enzyme does not oxidize uroporphyrinogen III
-
-
?
additional information
?
-
-
the enzyme cannot oxidize protoporphyrinogen IX
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
?
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
-
?
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
?
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
-
?
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
-
?
coproporphyrinogen III + 3 O2
coproporphyrin III + 3 H2O2
-
-
-
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
-
-
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
12fold higher catalytic efficiency with coproporphyrinogen III compared to protoporphyrinogen as substrate
-
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
-
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
12fold higher catalytic efficiency with coproporphyrinogen III compared to protoporphyrinogen as substrate
-
-
?
protoporphyrinogen IX + 3 O2
protoporphyrin IX + 3 H2O2
-
-
-
?
protoporphyrinogen IX + 3 O2
protoporphyrin IX + 3 H2O2
-
-
-
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
-
-
-
-
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
20fold lower activity with protoporphyrinogen IX compared to coproporphyrinogen III
-
-
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
20fold lower activity with protoporphyrinogen IX compared to coproporphyrinogen III
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
protoporphyrinogen IX
-
acts as a competitive inhibitor of the coproporphyrinogen III to coproporphyrin oxidase activity of HemY
additional information
-
the enzyme is not inhibited by the diphenyl ether herbicide acifluorfen at 0.1 mM
-
additional information
-
the enzyme exhibits resistence to acifluorfen
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-[3-(furan-2-yl)-1H-pyrazol-5-yl]naphthalen-1-ol
-
i.e. VU0038882, 204.8% activity at 0.01 mM
-
2-[3-(furan-2-yl)-1H-pyrazol-5-yl]naphthalen-1-ol
-
i.e. VU0038882
-
2-[3-(furan-2-yl)-1H-pyrazol-5-yl]naphthalen-1-ol
-
i.e. VU0038882
-
2-[3-(furan-2-yl)-1H-pyrazol-5-yl]naphthalen-1-ol
-
i.e. VU0038882
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0077
protoporphyrinogen IX
Halothece sp. PCC7418
pH and temperature not specified in the publication
0.0091
protoporphyrinogen IX
pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.252
protoporphyrinogen IX
pH and temperature not specified in the publication
0.256
protoporphyrinogen IX
Halothece sp. PCC7418
pH and temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
27.7
protoporphyrinogen IX
pH and temperature not specified in the publication
33.2
protoporphyrinogen IX
Halothece sp. PCC7418
pH and temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.03774
acifluorfen
wild type enzyme at pH 7.5, temperature not specified in the publication
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000012
saflufenacil
Halothece sp. PCC7418
pH and temperature not specified in the publication
0.0000484
saflufenacil
Oscillatoria nigro-viridis
pH and temperature not specified in the publication
0.0000091
tiafenacil
Halothece sp. PCC7418
pH and temperature not specified in the publication
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
-
the enzyme is required for a late step in protoheme IX synthesis
metabolism
-
the enzyme is required for a late step in protoheme IX synthesis
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
53000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with acifluorfen, sitting drop vapor diffusion method, using 2.4 M ammonium phosphate dibasic, 0.1 M Tris-HCl pH 7.5
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F227R
the mutant exhibits slight decrease in catalysis compared to the wild type enzyme
I176A
the mutation leads to about 30fold decrease in catalytic efficiency compared to the wild type enzyme
K71A
the mutation leads to about 50fold decrease in catalytic efficiency compared to the wild type enzyme
P64A
the mutant exhibits a 14fold decrease in catalysis compared to the wild type enzyme
Y366N
the mutation leads to about 100fold decrease in catalytic efficiency compared to the wild type enzyme
K71A
-
the mutation leads to about 50fold decrease in catalytic efficiency compared to the wild type enzyme
-
F187W
-
the mutation inhibits the activation of the enzyme by VU0038882
M167F
-
the mutation inhibits the activation of the enzyme by VU0038882
N186F
-
the mutant exhibits increased baseline activity relative to the wild type enzyme
N186Y
-
the mutant exhibits increased baseline activity relative to the wild type enzyme
T183K
-
the mutation does not restrict enzyme function. The mutant does not respond to VU0038882 at concentrations up to 0.01 mM
F187W
-
the mutation inhibits the activation of the enzyme by VU0038882
-
M167F
-
the mutation inhibits the activation of the enzyme by VU0038882
-
N186F
-
the mutant exhibits increased baseline activity relative to the wild type enzyme
-
N186Y
-
the mutant exhibits increased baseline activity relative to the wild type enzyme
-
T183K
-
the mutation does not restrict enzyme function. The mutant does not respond to VU0038882 at concentrations up to 0.01 mM
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni2+ affinity column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Arabidopsis thaliana and Escherichia coli strain BT3
expressed in Escherichia coli BL21(DE3) cells
the enzyme gene is fused in its 3'-end to a polynucleotide encoding six histidine residues and expressed in both Escherichia coli BL21(DE3) cells and Bacillus subtilis 168A cells
expressed in Arabidopsis thaliana and Escherichia coli strain BT3
expressed in Arabidopsis thaliana and Escherichia coli strain BT3
Halothece sp. PCC7418
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Corrigall, A.V.; Siziba, K.B.; Maneli, M.H.; Shephard, E.G.; Ziman, M.; Dailey, T.A.; Dailey, H.A.; Kirsch, R.E.; Meissner, P.N.
Purification of and kinetic studies on a cloned protoporphyrinogen oxidase from the aerobic bacterium Bacillus subtilis
Arch. Biochem. Biophys.
358
251-256
1998
Bacillus subtilis
brenda
Qin, X.; Sun, L.; Wen, X.; Yang, X.; Tan, Y.; Jin, H.; Cao, Q.; Zhou, W.; Xi, Z.; Shen, Y.
Structural insight into unique properties of protoporphyrinogen oxidase from Bacillus subtilis
J. Struct. Biol.
170
76-82
2010
Bacillus subtilis (P32397), Bacillus subtilis 168 (P32397)
brenda
Hobbs, C.; Dailey, H.A.; Shepherd, M.
The HemQ coprohaem decarboxylase generates reactive oxygen species: implications for the evolution of classical haem biosynthesis
Biochem. J.
473
3997-4009
2016
Staphylococcus aureus
brenda
Hansson, M.; Gustafsson, M.C.; Kannangara, C.G.; Hederstedt, L.
Isolated Bacillus subtilis HemY has coproporphyrinogen III to coproporphyrin III oxidase activity
Biochim. Biophys. Acta
1340
97-104
1997
Bacillus subtilis (P32397), Bacillus subtilis 168 (P32397)
brenda
Hansson, M.; Hederstedt, L.
Cloning and characterization of the Bacillus subtilis hemEHY gene cluster, which encodes protoheme IX biosynthetic enzymes
J. Bacteriol.
174
8081-8093
1992
Bacillus subtilis, Bacillus subtilis 3G18
brenda
Hansson, M.; Hederstedt, L.
Bacillus subtilis HemY is a peripheral membrane protein essential for protoheme IX synthesis which can oxidize coproporphyrinogen III and protoporphyrinogen IX
J. Bacteriol.
176
5962-5970
1994
Bacillus subtilis, Bacillus subtilis 3G18
brenda
Lobo, S.A.; Scott, A.; Videira, M.A.; Winpenny, D.; Gardner, M.; Palmer, M.J.; Schroeder, S.; Lawrence, A.D.; Parkinson, T.; Warren, M.J.; Saraiva, L.M.
Staphylococcus aureus haem biosynthesis: characterisation of the enzymes involved in final steps of the pathway
Mol. Microbiol.
97
472-487
2015
Staphylococcus aureus
brenda
Dailey, H.A.; Gerdes, S.; Dailey, T.A.; Burch, J.S.; Phillips, J.D.
Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrin
Proc. Natl. Acad. Sci. USA
112
2210-2215
2015
Bacillus subtilis
brenda
Klimka, A.; Mertins, S.; Nicolai, A.K.; Rummler, L.M.; Higgins, P.G.; Guenther, S.D.; Tosetti, B.; Krut, O.; Kroenke, M.
Epitope-specific immunity against Staphylococcus aureus coproporphyrinogen III oxidase
NPJ Vaccines
6
11
2021
Staphylococcus aureus (A0A3M8V9D3), Staphylococcus aureus USA300 (A0A3M8V9D3)
brenda
Yoon, J.; Han, Y.; Ahn, Y.O.; Hong, M.K.; Sung, S.K.
Characterization of HemY-type protoporphyrinogen IX oxidase genes from cyanobacteria and their functioning in transgenic Arabidopsis
Plant Mol. Biol.
101
561-574
2019
Oscillatoria nigro-viridis (K9VK16), Halothece sp. PCC7418 (K9Y873), Oscillatoria nigro-viridis PCC7112 (K9VK16)
brenda
Surdel, M.C.; Horvath, D.J.; Lojek, L.J.; Fullen, A.R.; Simpson, J.; Dutter, B.F.; Salleng, K.J.; Ford, J.B.; Jenkins, J.L.; Nagarajan, R.; Teixeira, P.L.; Albertolle, M.; Georgiev, I.S.; Jansen, E.D.; Sulikowski, G.A.; Lacy, D.B.; Dailey, H.A.; Skaar, E.P.
Antibacterial photosensitization through activation of coproporphyrinogen oxidase
Proc. Natl. Acad. Sci. USA
114
E6652-E6659
2017
Bacillus anthracis, Bacillus subtilis, Staphylococcus aureus, Cutibacterium acnes, Staphylococcus epidermidis, Staphylococcus haemolyticus, Staphylococcus lugdunensis, Staphylococcus aureus USA300
brenda
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